scispace - formally typeset
P

Paul van der Schoot

Researcher at Eindhoven University of Technology

Publications -  122
Citations -  5472

Paul van der Schoot is an academic researcher from Eindhoven University of Technology. The author has contributed to research in topics: Liquid crystal & Percolation threshold. The author has an hindex of 32, co-authored 122 publications receiving 4819 citations. Previous affiliations of Paul van der Schoot include Utrecht University & Claude Bernard University Lyon 1.

Papers
More filters
Journal ArticleDOI

Probing the Solvent-Assisted Nucleation Pathway in Chemical Self-Assembly

TL;DR: In this paper, the authors spectroscopically monitored a nucleation process in the self-assembly of p-conjugated molecules into helical supramolecular fibrillar structures.
Journal ArticleDOI

Ion-association complexes unite classical and non-classical theories for the biomimetic nucleation of calcium phosphate

TL;DR: A combination of in situ investigations are presented, which show that for the crystallization of calcium phosphate these nanometre-sized units are in fact calcium triphosphate complexes and demonstrate how the existence of these complexes lowers the energy barrier to nucleation and unites classical and non-classical nucleation theories.
Journal ArticleDOI

How to distinguish isodesmic from cooperative supramolecular polymerisation

TL;DR: It was found that for a rapid and unambiguous determination of the self-assembly mechanism and its thermodynamic parameters, temperature-dependent measurements are more appropriate.
Journal ArticleDOI

Supramolecular p -- n-Heterojunctions by Co-Self-Organization of Oligo(p-phenylene Vinylene) and Perylene Bisimide Dyes

TL;DR: The well-defined co-aggregated dyes presented here exhibit photoinduced electron transfer on subpicosecond time scale, and thus, these supramolecular entities might serve as valuable nanoscopic functional units.
Journal ArticleDOI

Classical Nucleation Theory of Virus Capsids

TL;DR: expression for the size of the critical capsid, the lag time, and the steady-state nucleation rate of capsids, and how they depend on both protein concentration and binding energy are found, explaining why capsid nucleation is a sensitive function of the ambient conditions.